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Information on EC 2.7.7.41 - phosphatidate cytidylyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P53230
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2.7.7.41 phosphatidate cytidylyltransferaseSpecify your search results
Word Map
- 2.7.7.41
- phospholipid
- phosphatidylinositol
- phosphatidylglycerol
- cardiolipin
- cds1
- liponucleotide
-
raetz
-
phosphatidyltransferase
-
diphosphate-diacylglycerol
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
cdp-diacylglycerol synthase, cdp-dg, phosphatidate cytidylyltransferase, tam41, cdp-dag synthase, tamm41, ctp:phosphatidate cytidylyltransferase, cdp-diglyceride synthetase, tbcds, cdp-dg synthase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CDP-DAG synthase
CDP-DG
-
-
-
-
CDP-DG synthetase
-
-
-
-
CDP-diacylglyceride synthetase
-
-
-
-
CDP-diacylglycerol synthase
CDP-diglyceride pyrophosphorylase
-
-
-
-
CDP-diglyceride synthetase
-
-
-
-
CDPdiglyceride pyrophosphorylase
-
-
-
-
CDS
CTP-diacylglycerol synthetase
-
-
-
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CTP:1,2-diacylglycerophosphate-cytidyl transferase
-
-
-
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CTP:phosphatidate cytidylyltransferase
-
-
-
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cytidine diphosphoglyceride pyrophosphorylase
-
-
-
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cytidylyltransferase, phosphatidate
-
-
-
-
DAG synthetase
-
-
-
-
phosphatidate cytidyltransferase
-
-
-
-
phosphatidic acid cytidylyltransferase
-
-
-
-
CDP-DAG synthase
-
-
-
-
CDP-diacylglycerol synthase
-
-
-
-
CDS
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CTP + phosphatidate = diphosphate + CDP-diacylglycerol
sequential bi-bi reaction: CDPdiacylglycerol synthase binds to CTP prior to phosphatidate and diphosphate is released prior to CDPdiacylglycerol in the reaction sequence
-
CTP + phosphatidate = diphosphate + CDP-diacylglycerol
sequential bi bi reaction mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
CTP:phosphatidate cytidylyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY
9067-83-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CTP + 1-palmitoyl-2-[12-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]dodecanoyl]-sn-glycero-3-phosphate
diphosphate + CDP-1-palmitoyl-2-[12-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]dodecanoyl]glycerol
i.e. commercial substrate NBD-PA
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
NBD-phosphatidate
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
equilibrium constant is 0.001. Reverse reaction is favored in vitro
-
-
r
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
the enzyme is involved in the regulation of phospholipid metabolism
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
regulation of phospholipid biosynthetic enzymes by the level of CDP-diacylglycerol synthase activity
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
-
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
the enzyme is involved in the regulation of phospholipid metabolism
-
-
?
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
-
regulation of phospholipid biosynthetic enzymes by the level of CDP-diacylglycerol synthase activity
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
diphosphate
-
2.5 mM, 80% inhibition of purified enzyme, noncompetitive with respect to CTP and phosphatidic acid
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.067
1-palmitoyl-2-[12-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]dodecanoyl]-sn-glycero-3-phosphate
pH 7.5, 30°C
0.067
phosphatidate
NBD-phosphatidate, pH and temperature not specified in the publication
0.076
CTP
with NBD-phosphatidate, pH and temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8.5
-
pH 6.0: 70% of maximal activity, pH 8.5: about 70% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
isoform Tam41 directly catalyzes the formation of CDP-diacylglycerol from phosphatidic acid in the mitochondrial inner membrane
additional information
isoform Cds1 is an ER-resident protein
-
enzyme is associated with both, the mitochondria and the endoplasmic reticulum
additional information
subcellular localization analysis of CDP-diacylglycerol synthases in yeast
-
additional information
subcellular localization analysis of CDP-diacylglycerol synthases in yeast
-
additional information
-
subcellular localization analysis of CDP-diacylglycerol synthases in yeast
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
both CDP-diacylglycerol synthases Tam41 and Cds1 are highly conserved proteins, yet their origins seem to be different. The N-terminal portion of Tam41 possesses the NTase (Nucleotide Transferase) fold, which is consistent with the CDP-DAG synthase function of Tam41. In contrast, Cds1 exhibits the CDP-DAG synthase i.e. NTase activity, yet it does not contain the NTase fold. Cds1 and Tam41 have developed their own commitment to lipid biosynthetic pathways operating in two evolutionary distinct organelles, the endoplasmic reticulum and mitochondria, during evolution of eukaryotic cells
malfunction
knockout mutant DELTAtam41 cells show severe growth defects on fermentable or non-fermentable media at high temperature, steady-state levels of cytochrome c1 of complex III and cytochrome oxidase subunit IV (Cox4) of complex IV are decreased in the mutant cells. Overexpression of Art5 (a arrestin-related trafficking adaptor family member) restores the temperature-sensitive growth defects of DELTAtam41 cells completely on fermentable media but only partly on non-fermentable media, which renders the cell growth dependent on mitochondrial respiration. Overexpression of both Cds1 and Art5 rescues growth defects of pgs1DELTAtam41DELTA cells. The growth defects of DELTAtam41 at elevated temperature are suppressed by the simultaneous deletion of the ITR1 gene
metabolism
CDP-diacylglycerol synthase Cds1 resides in the endoplasmic reticulum but not in mitochondria, while CDP-diacylglycerol synthase Tam41, a highly conserved mitochondrial maintenance protein, directly catalyzes the formation of CDP-DAG from phosphatidate in the mitochondrial inner membrane
physiological function
metabolism
-
the enzyme is critical for maintaining phosphoinositide levels during phospholipase C signaling
physiological function
inositol depletion by overexpressing an arrestin-related protein Art5 partially restores the defects of cell growth and cardiolipin synthesis in the absence of Tam41
physiological function
the CDP-diacylglycerol synthase Tam41 is required for cardiolipin biosynthesis in mitochondria
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
114000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
two polypeptides of 54000 Da and 56000 Da are detected by SDS-PAGE, it is possible that the 54000 Da subunit is a proteolysis product of the 56000 Da subunit
additional information
-
two distinct protein bands of 45000 Da and 19000 Da are detected by SDS-PAGE, it is yet unclear whether this represents simple aggregation of two unrelated proteins in a monomer dimer relationship, or whether the enzyme has two distinct subunits present in a 1:4 molar ratio
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D220A
site-directed mutagenesis of TAM41, catalytically inactive mutant
Y130A
site-directed mutagenesis of TAM41, catalytically inactive mutant
C102Y
mutation is the molecular basis for the inositol excretion phenotype
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the solubilized protein is quite labile. Its stability is markedly enhanced by exchange dialysis against 10% glycerol, 20% propylene glycol, 25 mM cacodylate buffer, pH 6.5, 10 mM MgCl2
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, in presence of 1 mM CTP the purified enzyme is 90-100% stable for at least 3 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Carman, G.M.; Kelley, M.J.
CDPdiacylglycerol synthase from yeast
Methods Enzymol.
209
242-247
1992
Saccharomyces cerevisiae
Kelley, M.J.; Carman, G.M.
Purification and characterization of CDP-diacylglycerol synthase from Saccharomyces cerevisiae
J. Biol. Chem.
262
14563-14570
1987
Saccharomyces cerevisiae
Belendiuk, G.; Mangnall, D.; Tung, B.; Westley, J.; Getz, G.S.
CTP-phosphatidic acid cytidyltransferase from Saccharomyces cerevisiae. Partial purification, characterization, and kinetic behavior
J. Biol. Chem.
253
4555-4565
1978
Saccharomyces cerevisiae
Dowhan, W.
CDP-diacylglycerol synthase of microorganisms
Biochim. Biophys. Acta
1348
157-165
1997
Saccharomyces cerevisiae, Escherichia coli
Shen, H.; Heacock, P.N.; Clancey, C.J.; Dowhan, W.
The CDS1 gene encoding CDP-diacylglycerol synthase in Saccharomyces cerevisiae is essential for cell growth
J. Biol. Chem.
271
789-795
1996
Saccharomyces cerevisiae (P38221), Saccharomyces cerevisiae
Shen, H.; Dowhan, W.
Regulation of phospholipid biosynthetic enzymes by the level of CDP-diacylglycerol synthase activity
J. Biol. Chem.
272
11215-11220
1997
Saccharomyces cerevisiae
Tamura, Y.; Harada, Y.; Nishikawa, S.; Yamano, K.; Kamiya, M.; Shiota, T.; Kuroda, T.; Kuge, O.; Sesaki, H.; Imai, K.; Tomii, K.; Endo, T.
Tam41 is a CDP-diacylglycerol synthase required for cardiolipin biosynthesis in mitochondria
Cell Metab.
17
709-718
2013
Saccharomyces cerevisiae (P38221), Saccharomyces cerevisiae (P53230), Saccharomyces cerevisiae
Blunsom, N.J.; Cockcroft, S.
CDP-diacylglycerol synthases (CDS) gateway to phosphatidylinositol and cardiolipin synthesis
Front. Cell Dev. Biol.
8
63
2020
Aeropyrum pernix, Saccharomyces cerevisiae, Drosophila melanogaster, Schizosaccharomyces pombe, Streptococcus mitis, Streptococcus oralis, Thermotoga maritima, Toxoplasma gondii, Trypanosoma brucei brucei, Eimeria falciformis, Arabidopsis thaliana (O04928), Arabidopsis thaliana (O49639), Arabidopsis thaliana (Q1PE48), Arabidopsis thaliana (Q94A03), Arabidopsis thaliana (Q9M001), Escherichia coli (P0ABG1), Danio rerio (Q3B7H2), Homo sapiens (Q92903), Homo sapiens (Q95674)
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